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Status of the cofactor identity in copper oxidative enzymes
Author(s) -
Klinman J.P.,
Dooley D.M.,
Duine J.A.,
Knowles P.F.,
Mondovi B.,
Villafranca J.J.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80431-2
Subject(s) - pyrroloquinoline quinone , chemistry , amine oxidase , cofactor , monooxygenase , active site , galactose oxidase , enzyme , biochemistry , copper protein , copper , oxidase test , stereochemistry , oxidative phosphorylation , organic chemistry , cytochrome p450
Much conflicting data have appeared in the literature regarding the nature of the active site structures responsible for catalysis in three classes of copper enzymes: the copper amine oxidases, dopamine β‐monooxygenase and galactose oxidase. Although pyrroloquinoline quinone has been proposed to be the active site cofactor in each instance, new findings indicate this is not the case. Instead, recently available data indicate a spectrum of strategies for substrate activation, which range from direct metal catalysis (dopamine β‐monooxygenase) to the involvement of protein‐derived radicals (galactose oxidase) and protein‐derived quinones (copper amine oxidases).